Evidence map›Paper›PMID 26824029›Full record

ArticleTranslation (Austin, Tex.)

Ribosomal protein uS19 mutants reveal its role in coordinating ribosome structure and function.

Alicia M Bowen, Sharmishtha Musalgaonkar, Christine A Moomau, Suna P Gulay, Mary Mirvis, Jonathan D Dinman

Open access · hybridAbstract read
In one paragraph

Article in Translation (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.5field-weighted citation impact, top 33% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 26 citations in OpenAlex.

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  11. Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Alicia M BowenDepartment of Chemistry and Biochemistry; University of Maryland ; College Park, MD USA.
Sharmishtha MusalgaonkarDepartment of Cell Biology and Molecular Genetics; University of Maryland ; College Park, MD USA.
Christine A MoomauDepartment of Cell Biology and Molecular Genetics; University of Maryland ; College Park, MD USA.
Suna P GulayDepartment of Cell Biology and Molecular Genetics; University of Maryland ; College Park, MD USA.
Mary MirvisDepartment of Cell Biology and Molecular Genetics; University of Maryland ; College Park, MD USA.
Jonathan D DinmanDepartment of Cell Biology and Molecular Genetics; University of Maryland ; College Park, MD USA.
University of Maryland, College Park · US

Funding

X-linked Dyskeratosis Congenita and Ribosomal FrameshiftingR01HL119439 · NHLBI · UNIV OF MARYLAND, COLLEGE PARK · PI DINMAN, JONATHAN D, RUGGERO, DAVIDE · 2014 to 2017
$2.8M
Regulation of programmed -1 ribosomal frameshifting by micro-RNAsR01GM117177 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI DINMAN, JONATHAN D · 2015 to 2018
$1.2M
NHLBI NIH HHS R01 HL119439NIGMS NIH HHS R01 GM117177
6 · The paper itself

Abstract

Prior studies identified allosteric information pathways connecting functional centers in the large ribosomal subunit to the decoding center in the small subunit through the B1a and B1b/c intersubunit bridges in yeast. In prokaryotes a single SSU protein, uS13, partners with H38 (the A-site finger) and uL5 to form the B1a and B1b/c bridges respectively. In eukaryotes, the SSU component was split into 2 separate proteins during the course of evolution. One, also known as uS13, participates in B1b/c bridge with uL5 in eukaryotes. The other, called uS19 is the SSU partner in the B1a bridge with H38. Here, polyalanine mutants of uS19 involved in the uS19/uS13 and the uS19/H38 interfaces were used to elucidate the important amino acid residues involved in these intersubunit communication pathways. Two key clusters of amino acids were identified: one located at the junction between uS19 and uS13, and a second that appears to interact with the distal tip of H38. Biochemical analyses reveal that these mutations shift the ribosomal rotational equilibrium toward the unrotated state, increasing ribosomal affinity for tRNAs in the P-site and for ternary complex in the A-site, and inhibit binding of the translocase, eEF2. These defects in turn affect specific aspects of translational fidelity. These findings suggest that uS19 plays a critical role as a conduit of information exchange between the large and small ribosomal subunits directly through the B1a, and indirectly through the B1b/c bridges.

Indexed as

intersubunit bridgesribosometranslational fidelityuS19yeast

Identifiers

PMID26824029
PMCPMC4721500
OpenAlexW2253871728

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.